Evidence map›Paper›PMID 22564751›Full record

ArticleMitochondrion2012

Multiple proteins with essential mitochondrial functions have glycosylated isoforms.

Amanda R Burnham-Marusich, Patricia M Berninsone

Open access · greenAbstract read
In one paragraph

Article in Mitochondrion, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  6. bioRxiv : the preprint server for biology · 2024
    Article
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  10. Review
  11. A broadly active fucosyltransferase LmjFUT1 whose mitochondrial localization and activity are essential in parasiticProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Article
  14. Review
  15. MitochondrialThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Amanda R Burnham-MarusichBiology Department, University of Nevada Reno, 1664 N. Virginia St., MS-314, Reno, NV 89557, USA. amanda.marusich@gmail.com
Patricia M Berninsone
University of Nevada, Reno · US

Funding

Outreach/Diversity/Pipeline ProjectP20GM103440 · NIGMS · UNIVERSITY OF NEVADA RENO · PI Eduardo A Robleto · 2012 to 2026
$58.0M
UNDERGRADUATE RESEARCH AND TRAININGP20RR016464 · NCRR · UNIVERSITY OF NEVADA RENO · PI KENYON, JAMES L · 2001 to 2011
$30.3M
Cell Biology of Signaling across MembranesP20GM103554 · NIGMS · UNIVERSITY OF NEVADA RENO · PI VON BARTHELD, CHRISTOPHER S · 2012 to 2016
$8.0M
CELL BIOLOGY OF SIGNALING ACROSS MEMBRANESP20RR024210 · NCRR · UNIVERSITY OF NEVADA RENO · PI VON BARTHELD, CHRISTOPHER S · 2011 to 2011
$2.1M
Acquisition of a Hybrid LC/MS/MS to Enhance Research in NevadaS10RR023587 · NCRR · UNIVERSITY OF NEVADA RENO · PI QUILICI, DAVID ROGER · 2009 to 2009
$472k
NCRR NIH HHS P20 RR-016464NCRR NIH HHS P20 RR016464NCRR NIH HHS P20 RR024210NCRR NIH HHS S10 RR023587NCRR NIH HHS S10RR023587NIGMS NIH HHS GM103440NIGMS NIH HHS GM103554NIGMS NIH HHS P20 GM103440NIGMS NIH HHS P20 GM103554
6 · The paper itself

Abstract

Nucleocytosolic and secreted proteins are commonly glycosylated. However, reports of glycosylated mitochondrial proteins are rare. Using lectin chromatography on bovine heart, we detected low-abundance glycoforms of nuclear-encoded proteins with well-established mitochondrial function: pyruvate dehydrogenase E1α, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, ADP/ATP translocase, ATP synthase d and oligomycin sensitivity-conferring protein. Notably, the latter two have been previously detected at the plasma membrane. Our findings indicate that glycosylation of classic mitochondrial proteins may be more common than previously appreciated. We discuss the implication that glycosylation could represent an unexplored mechanism for regulating these proteins' functions within mitochondria or at extra-mitochondrial locations.

Indexed as

AnimalsCattleChromatographyGlycoproteinsLectinsMitochondriaMitochondrial ProteinsMyocardiumProtein IsoformsGlycoproteinsLectinsMitochondrial ProteinsProtein Isoforms

Identifiers

PMID22564751
PMCPMC3595188
OpenAlexW1997814558

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.